› 5vnn

X-ray diffraction
2.5Å resolution

Crystal structure of Sec23a/Sec24a/Sec22 complexed with 4-phenylbutyric acid (50mM soaking)

Released:
DOI: 10.2210/pdb5vnn/pdb
PDB entry 5vnn coloured by chain, front view.
PDB entry 5vnn coloured by chain, side view.
PDB entry 5vnn coloured by chain, top view.
Source organisms:
Primary publication:
ER retention is imposed by COPII protein sorting and attenuated by 4-phenylbutyrate.
Ma W, Goldberg E, Goldberg J
OpenAccess logo Elife 6 (2017)
PMID: 28594326

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-517653 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Protein transport protein Sec23A Chain: A
Molecule details ›
Chain: A
Length: 764 amino acids
Theoretical weight: 86.18 KDa
Source organism: Homo sapiens
Expression system: Insect cell expression vector pTIE1
UniProt:
  • Canonical: Q15436 (Residues: 1-764; Coverage: 100%)
Gene name: SEC23A
Sequence domains:
Structure domains:
Protein transport protein Sec24A Chain: B
Molecule details ›
Chain: B
Length: 748 amino acids
Theoretical weight: 84.34 KDa
Source organism: Homo sapiens
Expression system: Insect cell expression vector pTIE1
UniProt:
  • Canonical: O95486 (Residues: 346-1093; Coverage: 68%)
Gene name: SEC24A
Sequence domains:
Structure domains:
Vesicle-trafficking protein SEC22b Chain: C
Molecule details ›
Chain: C
Length: 157 amino acids
Theoretical weight: 18.03 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: O08547 (Residues: 1-157; Coverage: 73%)
Gene names: Sec22b, Sec22l1
Sequence domains:
Structure domains: Longin domain

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand CLT 1 x CLT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2
Unit cell:
a: 148.016Å b: 97.715Å c: 128.967Å
α: 90° β: 89.59° γ: 90°
R-values:
R R work R free
0.212 0.21 0.25
Expression systems:
  • Insect cell expression vector pTIE1
  • Escherichia coli

Quick links

Citations

12 review citations

Pharmacological targeting of endoplasmic reticulum stress in disease.
Marciniak et al. (2022)
11 more

3 mentions without citation

ER retention is imposed by COPII protein sorting and attenuated by 4-phenylbutyrate.
Ma et al. (2017)
2 more